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Q98ES7 (PUR9_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:mlr4101
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP-Rule MF_00139

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 538538Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192116

Sequences

Sequence LengthMass (Da)Tools
Q98ES7 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 99A385431FB05517

FASTA53856,197
        10         20         30         40         50         60 
MAVAAKNIPA PDLVPVRRAL LSVFDKTGLI DFARALAAAG VELVSTGGTA KAIAEAGLAV 

        70         80         90        100        110        120 
RDVSELTGFP EIMDGRVKTL HPSVHGALLG VRDDPEHAAA MRKYGIEPID LLVSNLYPFE 

       130        140        150        160        170        180 
EVRRSGADYA AIVENIDIGG PAMIRASAKN HAYVAIVTDP GDYASVLNAL EMNIGSLSLD 

       190        200        210        220        230        240 
FRKKLAAKAF ARTATYDAAI SGWFAEALEI EHPTWRAFGG RLTEVMRYGE NPHQSAGFYV 

       250        260        270        280        290        300 
NGDKRPGVAT ARQLQGKQLS YNNINDTDAA FELAGEFDPS RSAAVAIIKH ANPCGVAEGT 

       310        320        330        340        350        360 
SLKSAYAKAL ACDPVSAFGG IVAVNRTLDA EAAEDIVKTF TEVIIAPDAT DEAAAIVAAK 

       370        380        390        400        410        420 
KNLRLLVTGG LPDPRSPGTT VKSVAGGLLV QGRDNAVVDD LELKVVTKRA PTPAEMADLK 

       430        440        450        460        470        480 
FAFRVAKHVK SNAIVYAKDG ATVGIGAGQM SRVDSSRIAA RKALDAAEAA GMTEPLTTGS 

       490        500        510        520        530 
VVASDAFFPF ADGLLAAVAA GATAVIQPGG SMNDKDVIAA ADEHGIAMVF TGVRHFRH 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB50840.1.
RefSeqNP_105054.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ98ES7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mlr4101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB50840; BAB50840; BAB50840.
GeneID1227715.
KEGGmlo:mlr4101.
PATRIC22480713. VBIMesLot2464_3244.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-3197-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_RHILO
AccessionPrimary (citable) accession number: Q98ES7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: October 1, 2001
Last modified: February 19, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways